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. 1980 Feb;141(2):431–435. doi: 10.1128/jb.141.2.431-435.1980

Periplasmic maltose-binding protein confers specificity on the outer membrane maltose pore of Escherichia coli.

M W Heuzenroeder, P Reeves
PMCID: PMC293644  PMID: 6444941

Abstract

ompB mutants of Escherichia coli K-12 are markedly deficient in porin in their outer membrane. This results in a decreased rate of uptake for many substrates: the maltose pore (lambda receptor) can in some circumstances, in the absence of the periplasmic maltose-binding protein, compensate for the consequent defects in permeability to lactose, mannitol, glycylglycyl-L-valine, and tri-L-ornithine. It is postulated that the maltose-binding protein associates with the maltose pore and confers on it the specificity for maltose, and that the absence of the maltose-binding protein leaves the pore open and results in enhanced transmembrane diffusion of molecules other than maltose. This paper presents evidence to support this hypothesis.

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Selected References

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